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Q5R880

- PLA2R_PONAB

UniProt

Q5R880 - PLA2R_PONAB

Protein

Secretory phospholipase A2 receptor

Gene

PLA2R1

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 54 (01 Oct 2014)
      Sequence version 2 (13 Nov 2007)
      Previous versions | rss
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    Functioni

    Receptor for secretory phospholipase A2 (sPLA2). Also able to bind to snake PA2-like toxins. Although its precise function remains unclear, binding of sPLA2 to its receptor participates in both positive and negative regulation of sPLA2 functions as well as clearance of sPLA2. Binding of sPLA2-IB/PLA2G1B induces various effects depending on the cell type, such as activation of the mitogen-activated protein kinase (MAPK) cascade to induce cell proliferation, the production of lipid mediators, selective release of arachidonic acid in bone marrow-derived mast cells. In neutrophils, binding of sPLA2-IB/PLA2G1B can activate p38 MAPK to stimulate elastase release and cell adhesion. May be involved in responses in proinflammatory cytokine productions during endotoxic shock. Also has endocytic properties and rapidly internalizes sPLA2 ligands, which is particularly important for the clearance of extracellular sPLA2s to protect their potent enzymatic activities. The soluble secretory phospholipase A2 receptor form is circulating and acts as a negative regulator of sPLA2 functions by blocking the biological functions of sPLA2-IB/PLA2G1B and sPLA2-X/PLA2G10 By similarity.By similarity

    GO - Molecular functioni

    1. carbohydrate binding Source: InterPro
    2. phospholipase binding Source: UniProtKB
    3. receptor activity Source: UniProtKB

    GO - Biological processi

    1. cytokine production Source: UniProtKB
    2. oxidative stress-induced premature senescence Source: UniProtKB
    3. positive regulation of arachidonic acid secretion Source: UniProtKB
    4. positive regulation of DNA damage response, signal transduction by p53 class mediator Source: UniProtKB
    5. reactive oxygen species metabolic process Source: UniProtKB
    6. receptor-mediated endocytosis Source: UniProtKB
    7. replicative senescence Source: UniProtKB

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Endocytosis

    Keywords - Ligandi

    Lectin

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Secretory phospholipase A2 receptor
    Short name:
    PLA2-R
    Short name:
    PLA2R
    Alternative name(s):
    180 kDa secretory phospholipase A2 receptor
    M-type receptor
    Cleaved into the following chain:
    Soluble secretory phospholipase A2 receptor
    Short name:
    Soluble PLA2-R
    Short name:
    Soluble PLA2R
    Gene namesi
    Name:PLA2R1
    OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
    Taxonomic identifieri9601 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
    ProteomesiUP000001595: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW
    3. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Membrane, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222By similarityAdd
    BLAST
    Chaini23 – 14641442Secretory phospholipase A2 receptorPRO_0000311252Add
    BLAST
    Chaini23 – ?Soluble secretory phospholipase A2 receptorBy similarityPRO_0000311253

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi53 ↔ 66By similarity
    Disulfide bondi91 ↔ 108By similarity
    Glycosylationi95 – 951N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi180 ↔ 206By similarity
    Disulfide bondi194 ↔ 221By similarity
    Disulfide bondi262 ↔ 356By similarity
    Disulfide bondi332 ↔ 348By similarity
    Disulfide bondi408 ↔ 503By similarity
    Glycosylationi456 – 4561N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi480 ↔ 495By similarity
    Disulfide bondi619 ↔ 636By similarity
    Disulfide bondi701 ↔ 798By similarity
    Disulfide bondi776 ↔ 790By similarity
    Disulfide bondi842 ↔ 939By similarity
    Disulfide bondi916 ↔ 931By similarity
    Disulfide bondi1069 ↔ 1089By similarity
    Disulfide bondi1211 ↔ 1225By similarity
    Disulfide bondi1282 ↔ 1378By similarity
    Disulfide bondi1356 ↔ 1370By similarity

    Post-translational modificationi

    The secretory phospholipase A2 receptor form may be produced by the action of metalloproteinases. It contains all extracellular domains and only lacks transmembrane and cytosolic regions. It is however unclear whether this form is produced by proteolytic cleavage as suggested by some experiments, or by alternative splicing By similarity.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliQ5R880.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini23 – 13981376ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1420 – 146445CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei1399 – 141921HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini40 – 163124Ricin B-type lectinPROSITE-ProRule annotationAdd
    BLAST
    Domaini175 – 22349Fibronectin type-IIPROSITE-ProRule annotationAdd
    BLAST
    Domaini240 – 357118C-type lectin 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini387 – 504118C-type lectin 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini524 – 645122C-type lectin 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini675 – 799125C-type lectin 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini821 – 940120C-type lectin 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini967 – 1098132C-type lectin 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini1123 – 1234112C-type lectin 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini1259 – 1379121C-type lectin 8PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1437 – 14437Endocytosis signal

    Domaini

    C-type lectin domains 3-5 mediate the interaction with phospholipase PLA2G1B.By similarity
    The endocytosis signal probably mediates endocytosis via clathrin-coated pits.By similarity

    Sequence similaritiesi

    Contains 8 C-type lectin domains.PROSITE-ProRule annotation
    Contains 1 fibronectin type-II domain.PROSITE-ProRule annotation
    Contains 1 ricin B-type lectin domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    HOVERGENiHBG108261.
    InParanoidiQ5R880.
    KOiK06560.

    Family and domain databases

    Gene3Di2.10.10.10. 1 hit.
    3.10.100.10. 8 hits.
    InterProiIPR001304. C-type_lectin.
    IPR016186. C-type_lectin-like.
    IPR018378. C-type_lectin_CS.
    IPR016187. C-type_lectin_fold.
    IPR000562. FN_type2_col-bd.
    IPR000772. Ricin_B_lectin.
    [Graphical view]
    PfamiPF00040. fn2. 1 hit.
    PF00059. Lectin_C. 8 hits.
    [Graphical view]
    SMARTiSM00034. CLECT. 8 hits.
    SM00059. FN2. 1 hit.
    SM00458. RICIN. 1 hit.
    [Graphical view]
    SUPFAMiSSF50370. SSF50370. 1 hit.
    SSF56436. SSF56436. 8 hits.
    PROSITEiPS00615. C_TYPE_LECTIN_1. 3 hits.
    PS50041. C_TYPE_LECTIN_2. 8 hits.
    PS00023. FN2_1. 1 hit.
    PS51092. FN2_2. 1 hit.
    PS50231. RICIN_B_LECTIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q5R880-1 [UniParc]FASTAAdd to Basket

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    MLLSPSLLLP LLLLLGAPRG CAEGVAAALT PERLLEWQDK GIFVIQSESL     50
    KKCIQAGKSV LTLENCKQAN KHMLWKWVSN HGLFNIGGSG CLGLNFSAPE 100
    QPLSLYECDS TLVSLRWRCD RKMITGPLQY SVQVAHDNTV VASRKYFHKW 150
    ISYGSGGGDI CEYLHKDLHT IKGNAHGMPC MFPFQYNHQW HHECTREGRE 200
    DDLLWCATTS RYERDEKWGF CPDPTSAEVG CDTIWEKDLN SHICYQFNLL 250
    SSLSWSEAHS SCQMQGGALL SITDETEENF IREHMSSKTV EVWMGLNQLD 300
    EHAGWQWSDG TPLNYLNWSP EVNFEPFVED HCGTFSSFIP SAWRSRDCAS 350
    TLPYVCKKYL NHIDHEIVEK DAWKYYATHC EPGWNPYNRN CYKLQKEEKT 400
    WHEALRSCQA DNSALIDITS LAEVEFLVTL LGDENASETW IGLSSNKIPV 450
    SFEWSNDSSV IFTNWHTLEP QIFPNRSQLC VSAEQSEGHW KVKNCEETLF 500
    YVCKKAGHVL SDAESGCQEG WERHGGFCYK IDTVLRSFDQ ASSGYYCPPA 550
    LVTITNRFEQ AFITSLIGSV VKMKDSYFWI ALQDQNDTGE YTWKPAGQKP 600
    EPVQYTHWNA HQPRYSGGCV AMRGRHPPGR WEVKHCRHFK AMSLCKQPVE 650
    NQEKAEYEER WPFHPCYLDW ESEPGLASCF KVFHSEKVLM KRTWREAEAF 700
    CEEFGAHLAS FAHIEEENFV NELLYSKFNW TEERQFWIGF NKRNPLNAGS 750
    WEWSDRIPVV SSFLDNNYFG EDARNCAVYK ANKTLLPLHC GSKREWICKI 800
    PRDVKPKIPF WYQYDVPWLF YQDAEYLFHT FASEWLNFEF VCSWLHSDLL 850
    TIHSAHEQEF IHSKIKALSK YGASWWIGLQ EERANDEFRW RDGTPVIYQN 900
    WDTGRERPVN NQSQRCGFIS SITGLWGSEE CSVSMPSICK RKKVLLIEKK 950
    KDTPKQHGTC PKGWLYFNYK CLLLNIPKDP NSWKNWMHAQ HFCAEEGGTL 1000
    VAIESEVEQA FITMNLFGQT TNVWIGLQND DYETWLNGKP VVYSNWSPFD 1050
    IINIPSHNTT DVQKHIPLCA LLSSNPNFHF TGKWYFEDCG KEGYGFVCEK 1100
    MQDTSGHGVN TSDMYPMPNT LEYGNRTYKI INANMTWYAA IKTCLMHGTQ 1150
    LVSITDQYHQ SFLTVVLNRL GYAHWIGLFT TDNGLNFDWS DGTKSSFTFW 1200
    KDEESSLLGD CVFADTNGLW HSTACESFLQ GAICHVPPET RQSEHPELCS 1250
    ETSIPWIKFK SNCYSFSTVL DRMSFEAAHE FCKKEGSNLL TIKDEAENAF 1300
    LLEELFAFGS SVQMVWLNAQ FDGNNETIKW FDGTPTDQSN WGIRKPDTDY 1350
    FKPHHCVALR IPEGLQLSLC QEKKGFICKM EADIRTAEEL PEKGPSHSII 1400
    PLAVVLTLIV IVAICTLSFC IYKHNGGFFR RLAGFRNPYY PATNFSTVHL 1450
    EENILISDLE KSDQ 1464
    Length:1,464
    Mass (Da):168,437
    Last modified:November 13, 2007 - v2
    Checksum:i8D4DEA5A43CB1C8A
    GO

    Sequence cautioni

    The sequence CAH92030.1 differs from that shown. Reason: Erroneous termination at position 1366. Translated as Gln.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR859874 mRNA. Translation: CAH92030.1. Sequence problems.
    RefSeqiNP_001126180.1. NM_001132708.1.
    UniGeneiPab.11399.

    Genome annotation databases

    GeneIDi100173143.
    KEGGipon:100173143.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR859874 mRNA. Translation: CAH92030.1 . Sequence problems.
    RefSeqi NP_001126180.1. NM_001132708.1.
    UniGenei Pab.11399.

    3D structure databases

    ProteinModelPortali Q5R880.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100173143.
    KEGGi pon:100173143.

    Organism-specific databases

    CTDi 22925.

    Phylogenomic databases

    HOVERGENi HBG108261.
    InParanoidi Q5R880.
    KOi K06560.

    Family and domain databases

    Gene3Di 2.10.10.10. 1 hit.
    3.10.100.10. 8 hits.
    InterProi IPR001304. C-type_lectin.
    IPR016186. C-type_lectin-like.
    IPR018378. C-type_lectin_CS.
    IPR016187. C-type_lectin_fold.
    IPR000562. FN_type2_col-bd.
    IPR000772. Ricin_B_lectin.
    [Graphical view ]
    Pfami PF00040. fn2. 1 hit.
    PF00059. Lectin_C. 8 hits.
    [Graphical view ]
    SMARTi SM00034. CLECT. 8 hits.
    SM00059. FN2. 1 hit.
    SM00458. RICIN. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50370. SSF50370. 1 hit.
    SSF56436. SSF56436. 8 hits.
    PROSITEi PS00615. C_TYPE_LECTIN_1. 3 hits.
    PS50041. C_TYPE_LECTIN_2. 8 hits.
    PS00023. FN2_1. 1 hit.
    PS51092. FN2_2. 1 hit.
    PS50231. RICIN_B_LECTIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. The German cDNA consortium
      Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Kidney.

    Entry informationi

    Entry nameiPLA2R_PONAB
    AccessioniPrimary (citable) accession number: Q5R880
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 13, 2007
    Last sequence update: November 13, 2007
    Last modified: October 1, 2014
    This is version 54 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3